RPOB_RICRS
ID RPOB_RICRS Reviewed; 1373 AA.
AC A8GQW4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE Short=RNAP subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=Transcriptase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
GN Name=rpoB {ECO:0000255|HAMAP-Rule:MF_01321}; OrderedLocusNames=A1G_01035;
OS Rickettsia rickettsii (strain Sheila Smith).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=392021;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sheila Smith;
RA Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Dasch G., Eremeeva M.;
RT "Complete genome sequence of Rickettsia rickettsii.";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6; Evidence={ECO:0000255|HAMAP-Rule:MF_01321};
CC -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC and 1 omega subunit. When a sigma factor is associated with the core
CC the holoenzyme is formed, which can initiate transcription.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
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DR EMBL; CP000848; ABV75789.1; -; Genomic_DNA.
DR RefSeq; WP_012150397.1; NC_009882.1.
DR AlphaFoldDB; A8GQW4; -.
DR SMR; A8GQW4; -.
DR EnsemblBacteria; ABV75789; ABV75789; A1G_01035.
DR GeneID; 45538777; -.
DR KEGG; rri:A1G_01035; -.
DR HOGENOM; CLU_000524_4_0_5; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000006832; Chromosome.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.30.150.10; -; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR HAMAP; MF_01321; RNApol_bact_RpoB; 1.
DR InterPro; IPR042107; DNA-dir_RNA_pol_bsu_ext_1_sf.
DR InterPro; IPR019462; DNA-dir_RNA_pol_bsu_external_1.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR010243; RNA_pol_bsu_bac.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF10385; RNA_pol_Rpb2_45; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR TIGRFAMs; TIGR02013; rpoB; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Nucleotidyltransferase; Transcription;
KW Transferase.
FT CHAIN 1..1373
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000051980"
SQ SEQUENCE 1373 AA; 154258 MW; 90BEBC51AB42BFA6 CRC64;
MVSLRDNIEA QPLSHNRRIR KNFGHINLVA DIPNLIEIQK NSYEKNFLQL NIKDSERKNK
GLQSILNSIF PISDSSNVAN LEFVKYEFDT PKYDVEECSQ RSLSYAAPLK VTLRLSIWDI
DEDTGTREIK GIKEQEVYMG DIPLMTKNGT FIINGTERVV VSQMHRSPGV FFYHDEGKVH
SSGKLLYSAR VIPYRGSWLD LEFDAKDVIY FRIDRKRKLY ATTLLRAIGM STEEIIKFYY
NSVTYKLVKN KGWAVKFIPQ HITAHRLTSD LVDADTGNIL LKAGQKITPR LAKKYFGEGL
NNILVAHETL IGKYLSEDLR DPASDEVLAK IGEMITADML NVINDLKIKN VNVLVINPQS
GPYIRNTLFA DKNQDREAAL CDIFRVLRPG EPANIEAAES LFYNLFFDTE RYDLSEVGRI
KMNSRLELNI SEEVTVLTID DIKNIVRVLV ELKDGKGIID DIDHLGNRRV RSVGELIENQ
FRIGLVRMEK SVIERMSAGD VDTVMPHDLV NSKILVSVVK EFFSTSQLSQ FMDQTNPLSE
ITHKRRLSAL GPGGLSRDRA GFEVRDVHPT HYGRICPIET PEGQNIGLIN SMATYARINK
HGFIESPYRR VKDGCVTDEV VYLSAIEEGK YKIGQANSKI NKDGKLQGEF INCRVEGGNF
VMVEPYEVDF IDVTPMQVVS VAASLIPFLE NDDANRALMG SNMQRQAVPL IKTDAPFVGT
GVEGVVAKDS GASVLALHDG IVEQVDSNRI VIRTLEQKVD GSPSVDIYNL LKFQKSNHNT
CINQKPLVKV GHYVKKNDII ADGPSTDNGE IALGRNVLVA FLPWNGYNFE DSILISERIV
KEDVFTSIHI EEFEVIARDT RLGPEEITRD IPNVSEEALR HLDEVGIIYI GAEVKAGDIL
VGKVTPKSES PITPEEKLLR AIFGEKAFDV KDSSLHVPSG VSGTVVEVRV FSRRGVEKDQ
RAIAIEKQQI EKFAKDRDDE LEIIEHFVFS WLEKLLVGQV IINGPKQVKV GQTITTEMLK
GLSKGQFWQI TVEDANVMNE IEQIKTHYDE KKEALDKRFA TKVEKLQSGD DLPQGALKVV
KVFIATKHKL QPGDKMAGRH GNKGVISRIV PEEDMPFLED GTVVDIVLNP LGLPSRMNIG
QILETHLGWA SINLAKKIST LVKEYKNKHI GIEQIKKFLI ELYGENINSI LERPEEEIIA
FCKKVSKGVH FATPVFDGAK VQDVKDMLKL AGQDPSGQVK LIDGRTGEYF DRLVTVGQKY
LLKLHHLVDN KIHSRSIGPY SLVTQQPLGG KSHFGGQRFG EMECWALQAY GAAYTLQEML
TVKSDDVNGR IKTYDSIVRG ENNFESGIPE SFNVMIKEFR SLCLNVKLEV TSS
